Table 1.
Kinetic and binding parameters of AdiC variants
| Transport kinetics # | Binding (ITC) | ||
| AdiC variant | VMAX (pmol/μg· min) | KM (μM) | Apparent Kd (μM) |
| wild-type | 36, 64 | 31, 42 | 95, 97, 100, 122 |
| W293Y | 5.1, 8.7 | 122, 133 | no signal |
| N101A | 0.7, 0.8 | 93, 111 | no signal |
| N101D | 89, 101 | 110, 100 | 112 |
VMAX and KM values of each AdiC variant calculated from two independent protein preparations with 4 mM L-arginine inside the proteoliposomes. #, A representative experiment of each variant is shown in Fig. S2B. Apparent dissociation constants (Kd) of L-arginine-AdiC (wild type and mutants) binding were calculated from ITC measurements. The Kd values are presented for the indicated independent preparations of each variant. No heat flux in the calorimeter was recorded in two independent preparations of W293Y and N101A.